BEX2_HUMAN
ID BEX2_HUMAN Reviewed; 128 AA.
AC Q9BXY8; B2R574; D3DXA2; F5H7H5; Q5JVV9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein BEX2;
DE AltName: Full=Brain-expressed X-linked protein 2;
DE Short=hBex2;
GN Name=BEX2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15958283; DOI=10.1016/j.gene.2005.05.012;
RA Alvarez E., Zhou W., Witta S.E., Freed C.R.;
RT "Characterization of the Bex gene family in humans, mice, and rats.";
RL Gene 357:18-28(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mao Y., Xie Y., Zhou Z., Zhao W., Zhao S., Wang W., Huang Y., Wang S.,
RA Tang R., Chen X., Wu C.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH LMO2.
RX PubMed=16314316; DOI=10.1093/nar/gki964;
RA Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J.,
RA Qiang B., Liu Y.-J., Peng X.;
RT "Human Bex2 interacts with LMO2 and regulates the transcriptional activity
RT of a novel DNA-binding complex.";
RL Nucleic Acids Res. 33:6555-6565(2005).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19711341; DOI=10.1002/ijc.24866;
RA Naderi A., Liu J., Bennett I.C.;
RT "BEX2 regulates mitochondrial apoptosis and G1 cell cycle in breast
RT cancer.";
RL Int. J. Cancer 126:1596-1610(2010).
CC -!- FUNCTION: Regulator of mitochondrial apoptosis and G1 cell cycle in
CC breast cancer. Protects the breast cancer cells against mitochondrial
CC apoptosis and this effect is mediated through the modulation of BCL2
CC protein family, which involves the positive regulation of anti-
CC apoptotic member BCL2 and the negative regulation of pro-apoptotic
CC members BAD, BAK1 and PUMA. Required for the normal cell cycle
CC progression during G1 in breast cancer cells through the regulation of
CC CCND1 and CDKN1A. Regulates the level of PP2A regulatory subunit B and
CC PP2A phosphatase activity. {ECO:0000269|PubMed:19711341}.
CC -!- SUBUNIT: Interacts with OMP (By similarity). Interacts with LMO2,
CC possibly leading to regulate the transcriptional activity of a DNA-
CC binding complex containing LMO2. {ECO:0000250,
CC ECO:0000269|PubMed:16314316}.
CC -!- INTERACTION:
CC Q9BXY8; Q6PJH3: AKAP9; NbExp=3; IntAct=EBI-745073, EBI-11745576;
CC Q9BXY8; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-745073, EBI-11519926;
CC Q9BXY8; Q9H2G9: BLZF1; NbExp=6; IntAct=EBI-745073, EBI-2548012;
CC Q9BXY8; Q96GS4: BORCS6; NbExp=3; IntAct=EBI-745073, EBI-10193358;
CC Q9BXY8; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-745073, EBI-739580;
CC Q9BXY8; Q8NCU1: CCDC197; NbExp=3; IntAct=EBI-745073, EBI-750686;
CC Q9BXY8; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-745073, EBI-10961624;
CC Q9BXY8; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-745073, EBI-347573;
CC Q9BXY8; Q01850: CDR2; NbExp=3; IntAct=EBI-745073, EBI-1181367;
CC Q9BXY8; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-745073, EBI-739624;
CC Q9BXY8; Q9H9E3: COG4; NbExp=3; IntAct=EBI-745073, EBI-368382;
CC Q9BXY8; P78358: CTAG1B; NbExp=5; IntAct=EBI-745073, EBI-1188472;
CC Q9BXY8; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-745073, EBI-3867333;
CC Q9BXY8; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-745073, EBI-356015;
CC Q9BXY8; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-745073, EBI-742102;
CC Q9BXY8; A1L4K1: FSD2; NbExp=3; IntAct=EBI-745073, EBI-5661036;
CC Q9BXY8; P19883: FST; NbExp=3; IntAct=EBI-745073, EBI-1571188;
CC Q9BXY8; O75031: HSF2BP; NbExp=3; IntAct=EBI-745073, EBI-7116203;
CC Q9BXY8; Q16082: HSPB2; NbExp=3; IntAct=EBI-745073, EBI-739395;
CC Q9BXY8; Q9BS75: KLHL20; NbExp=3; IntAct=EBI-745073, EBI-10693436;
CC Q9BXY8; Q92876: KLK6; NbExp=3; IntAct=EBI-745073, EBI-2432309;
CC Q9BXY8; Q9Y448: KNSTRN; NbExp=3; IntAct=EBI-745073, EBI-373334;
CC Q9BXY8; P19012: KRT15; NbExp=3; IntAct=EBI-745073, EBI-739566;
CC Q9BXY8; P08727: KRT19; NbExp=3; IntAct=EBI-745073, EBI-742756;
CC Q9BXY8; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-745073, EBI-3044087;
CC Q9BXY8; Q15323: KRT31; NbExp=6; IntAct=EBI-745073, EBI-948001;
CC Q9BXY8; O76011: KRT34; NbExp=3; IntAct=EBI-745073, EBI-1047093;
CC Q9BXY8; O76015: KRT38; NbExp=3; IntAct=EBI-745073, EBI-1047263;
CC Q9BXY8; Q6A163: KRT39; NbExp=3; IntAct=EBI-745073, EBI-11958242;
CC Q9BXY8; Q6A162: KRT40; NbExp=3; IntAct=EBI-745073, EBI-10171697;
CC Q9BXY8; P02538: KRT6A; NbExp=3; IntAct=EBI-745073, EBI-702198;
CC Q9BXY8; O95678: KRT75; NbExp=3; IntAct=EBI-745073, EBI-2949715;
CC Q9BXY8; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-745073, EBI-10171774;
CC Q9BXY8; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-745073, EBI-1052037;
CC Q9BXY8; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-745073, EBI-10176379;
CC Q9BXY8; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-745073, EBI-14065470;
CC Q9BXY8; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-745073, EBI-18395721;
CC Q9BXY8; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-745073, EBI-3957694;
CC Q9BXY8; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-745073, EBI-3958099;
CC Q9BXY8; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-745073, EBI-11962084;
CC Q9BXY8; P80188: LCN2; NbExp=3; IntAct=EBI-745073, EBI-11911016;
CC Q9BXY8; O95751: LDOC1; NbExp=3; IntAct=EBI-745073, EBI-740738;
CC Q9BXY8; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-745073, EBI-741037;
CC Q9BXY8; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-745073, EBI-10178634;
CC Q9BXY8; P43356: MAGEA2B; NbExp=3; IntAct=EBI-745073, EBI-5650739;
CC Q9BXY8; Q1RN33: MAGEA4; NbExp=3; IntAct=EBI-745073, EBI-10194128;
CC Q9BXY8; Q99750: MDFI; NbExp=4; IntAct=EBI-745073, EBI-724076;
CC Q9BXY8; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-745073, EBI-2548751;
CC Q9BXY8; Q13064: MKRN3; NbExp=6; IntAct=EBI-745073, EBI-2340269;
CC Q9BXY8; Q6PF18: MORN3; NbExp=3; IntAct=EBI-745073, EBI-9675802;
CC Q9BXY8; Q96DV4: MRPL38; NbExp=3; IntAct=EBI-745073, EBI-720441;
CC Q9BXY8; Q4VC12: MSS51; NbExp=3; IntAct=EBI-745073, EBI-11599933;
CC Q9BXY8; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-745073, EBI-11522433;
CC Q9BXY8; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-745073, EBI-10172876;
CC Q9BXY8; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-745073, EBI-10271199;
CC Q9BXY8; O43482: OIP5; NbExp=3; IntAct=EBI-745073, EBI-536879;
CC Q9BXY8; O15496: PLA2G10; NbExp=3; IntAct=EBI-745073, EBI-726466;
CC Q9BXY8; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-745073, EBI-949255;
CC Q9BXY8; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-745073, EBI-302345;
CC Q9BXY8; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-745073, EBI-3957793;
CC Q9BXY8; Q96C74: ROPN1L; NbExp=3; IntAct=EBI-745073, EBI-9033237;
CC Q9BXY8; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-745073, EBI-748621;
CC Q9BXY8; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-745073, EBI-5235340;
CC Q9BXY8; O43610: SPRY3; NbExp=3; IntAct=EBI-745073, EBI-12290641;
CC Q9BXY8; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-745073, EBI-2212028;
CC Q9BXY8; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-745073, EBI-6872807;
CC Q9BXY8; Q9Y6A5: TACC3; NbExp=3; IntAct=EBI-745073, EBI-2554984;
CC Q9BXY8; Q13077: TRAF1; NbExp=3; IntAct=EBI-745073, EBI-359224;
CC Q9BXY8; Q12933: TRAF2; NbExp=6; IntAct=EBI-745073, EBI-355744;
CC Q9BXY8; P14373: TRIM27; NbExp=3; IntAct=EBI-745073, EBI-719493;
CC Q9BXY8; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-745073, EBI-5235829;
CC Q9BXY8; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-745073, EBI-11525489;
CC Q9BXY8; Q86UV6-2: TRIM74; NbExp=3; IntAct=EBI-745073, EBI-10259086;
CC Q9BXY8; Q15654: TRIP6; NbExp=3; IntAct=EBI-745073, EBI-742327;
CC Q9BXY8; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-745073, EBI-739895;
CC Q9BXY8; Q9UK41-2: VPS28; NbExp=3; IntAct=EBI-745073, EBI-12146727;
CC Q9BXY8; P17023: ZNF19; NbExp=3; IntAct=EBI-745073, EBI-12884200;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:16314316}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BXY8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXY8-2; Sequence=VSP_046808;
CC -!- TISSUE SPECIFICITY: Expressed in central nervous system, with high
CC level in pituitary, cerebellum and temporal lobe. Widely expressed in
CC breast cancer cell lines. {ECO:0000269|PubMed:15958283,
CC ECO:0000269|PubMed:19711341}.
CC -!- SIMILARITY: Belongs to the BEX family. {ECO:0000305}.
CC -!- CAUTION: Was named BEX1 by some authors. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BEX2ID44162chXq22.html";
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DR EMBL; AY833560; AAX40678.1; -; mRNA.
DR EMBL; AF251053; AAK34943.1; -; mRNA.
DR EMBL; AK312085; BAG35021.1; -; mRNA.
DR EMBL; AL133348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z70233; CAD24039.1; -; Genomic_DNA.
DR EMBL; CH471190; EAW54715.1; -; Genomic_DNA.
DR EMBL; CH471190; EAW54716.1; -; Genomic_DNA.
DR EMBL; BC015522; AAH15522.1; -; mRNA.
DR CCDS; CCDS14505.1; -. [Q9BXY8-1]
DR CCDS; CCDS55467.1; -. [Q9BXY8-2]
DR RefSeq; NP_001161871.1; NM_001168399.1. [Q9BXY8-2]
DR RefSeq; NP_001161872.1; NM_001168400.1.
DR RefSeq; NP_001161873.1; NM_001168401.1. [Q9BXY8-1]
DR RefSeq; NP_116010.1; NM_032621.3. [Q9BXY8-1]
DR AlphaFoldDB; Q9BXY8; -.
DR BioGRID; 124218; 107.
DR CORUM; Q9BXY8; -.
DR IntAct; Q9BXY8; 89.
DR MINT; Q9BXY8; -.
DR STRING; 9606.ENSP00000442521; -.
DR iPTMnet; Q9BXY8; -.
DR PhosphoSitePlus; Q9BXY8; -.
DR SwissPalm; Q9BXY8; -.
DR BioMuta; BEX2; -.
DR DMDM; 74752443; -.
DR MassIVE; Q9BXY8; -.
DR PaxDb; Q9BXY8; -.
DR PeptideAtlas; Q9BXY8; -.
DR PRIDE; Q9BXY8; -.
DR Antibodypedia; 44280; 87 antibodies from 18 providers.
DR DNASU; 84707; -.
DR Ensembl; ENST00000372674.5; ENSP00000361759.1; ENSG00000133134.12. [Q9BXY8-1]
DR Ensembl; ENST00000372677.8; ENSP00000361762.3; ENSG00000133134.12. [Q9BXY8-1]
DR Ensembl; ENST00000536889.1; ENSP00000442521.1; ENSG00000133134.12. [Q9BXY8-2]
DR GeneID; 84707; -.
DR KEGG; hsa:84707; -.
DR MANE-Select; ENST00000372677.8; ENSP00000361762.3; NM_032621.4; NP_116010.1.
DR UCSC; uc004eka.4; human. [Q9BXY8-1]
DR CTD; 84707; -.
DR DisGeNET; 84707; -.
DR GeneCards; BEX2; -.
DR HGNC; HGNC:30933; BEX2.
DR HPA; ENSG00000133134; Tissue enhanced (pituitary).
DR MIM; 300691; gene.
DR neXtProt; NX_Q9BXY8; -.
DR OpenTargets; ENSG00000133134; -.
DR PharmGKB; PA134977614; -.
DR VEuPathDB; HostDB:ENSG00000133134; -.
DR eggNOG; ENOG502RW3Y; Eukaryota.
DR GeneTree; ENSGT00940000153412; -.
DR HOGENOM; CLU_123122_1_0_1; -.
DR InParanoid; Q9BXY8; -.
DR OMA; PVLQYRW; -.
DR OrthoDB; 1532209at2759; -.
DR PhylomeDB; Q9BXY8; -.
DR TreeFam; TF337909; -.
DR PathwayCommons; Q9BXY8; -.
DR SignaLink; Q9BXY8; -.
DR BioGRID-ORCS; 84707; 16 hits in 671 CRISPR screens.
DR ChiTaRS; BEX2; human.
DR GeneWiki; BEX2; -.
DR GenomeRNAi; 84707; -.
DR Pharos; Q9BXY8; Tbio.
DR PRO; PR:Q9BXY8; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9BXY8; protein.
DR Bgee; ENSG00000133134; Expressed in endothelial cell and 182 other tissues.
DR ExpressionAtlas; Q9BXY8; baseline and differential.
DR Genevisible; Q9BXY8; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR007623; BEX.
DR InterPro; IPR021156; TF_A-like/BEX.
DR PANTHER; PTHR19430; PTHR19430; 1.
DR Pfam; PF04538; BEX; 1.
DR PIRSF; PIRSF008633; BEX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cell cycle; Cytoplasm; Methylation;
KW Nucleus; Reference proteome.
FT CHAIN 1..128
FT /note="Protein BEX2"
FT /id="PRO_0000229777"
FT REGION 107..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTZ8"
FT VAR_SEQ 1
FT /note="M -> MQKMVVCGAKCCGDAPHVENREEETARIGPGVM (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046808"
SQ SEQUENCE 128 AA; 15321 MW; F6302EC28F71D2A8 CRC64;
MESKEERALN NLIVENVNQE NDEKDEKEQV ANKGEPLALP LNVSEYCVPR GNRRRFRVRQ
PILQYRWDIM HRLGEPQARM REENMERIGE EVRQLMEKLR EKQLSHSLRA VSTDPPHHDH
HDEFCLMP
